title: Oligoethylene glycols prevent thermal aggregation of α-chymotrypsin in a temperature-dependent manner: implications for design guidelines.
abstract: Protein aggregation is problematic in various fields, where aggregation can frequently occur during routine experiments. This study showed that tetraethylene glycol (TEG) and tetraethylene glycol dimethyl ether (TEGDE) act as aggregation suppressors that have different unique properties from typical additives to prevent protein aggregation, such as arginine (Arg) and NaCl. Thermal aggregation of α-chymotrypsin was well suppressed with the addition of both TEG and TEGDE. Interestingly, the suppressive effects of Arg and NaCl on thermal aggregation were almost unchanged when temperature was shifted from 65°C to 85°C, whereas both TEG and TEGDE significantly decreased the aggregation rate with increasing temperature. Note that the effects of TEG and TEGDE were higher than Arg above 75°C. This temperature-dependent behavior of TEG and TEGDE provides a novel design guideline to develop aggregation suppressors for use at high temperature, i.e., the importance of the ethylene oxide group.
authors.affiliation: Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Tokyo, Japan.
authors.forename: Shunsuke
authors.initials: S
authors.lastname: Tomita
authors.forename: Yumiko
authors.initials: Y
authors.lastname: Tanabe
authors.forename: Kentaro
authors.initials: K
authors.lastname: Shiraki
mesh_terms: D002918:Chymotrypsin / Q000737:chemistry*; D002942:Circular Dichroism; D004492:Edetic Acid; D005026:Ethylene Glycols / Q000737:chemistry; D006358:Hot Temperature; D011092:Polyethylene Glycols / Q000737:chemistry*; D011489:Protein Denaturation
chemical_list: D005026:Ethylene Glycols; D011092:Polyethylene Glycols; C441631:tetraglyme; D004492:Edetic Acid; D002918:Chymotrypsin; C117608:alpha-chymotrypsin
keywords: arginine; oligoethylene glycols; protein aggregation; α-chymotrypsin